This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. D-alanylgriseoluteic acid (AGA) is a broad spectrum antibiotic produced by Pantoea agglomerans (aka Erwinia herbicola), an enterobacterial species that is known to produce a number of interesting antimicrobial compounds. P. agglomerans appears to deploy AGA to kill other microorganisms in its local environment thus enhancing its competitiveness. AGA has been shown particularly effective against gram positive organisms. Certain strains of P. agglomerans are also capable of causing serious infections in humans. Thus we are interested not only in the chemistry of AGA biosynthesis from the standpoint of assessing the development of AGA like molecules as therapeutics. Many of the other steps in AGA biosynthesis are uncharacterized or poorly characterized. The subject of this work EhpF appears to be a phenazine CoA ligase that, we speculate, activates a phenazine substrate for a condensation reaction that modifies the phenazine ring system. Determination of the structure of EhpF will permit a comparison with other CoA liagses and will facilitate the design of specific biochemical experiments.